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Nico Bruns - One of the best experts on this subject based on the ideXlab platform.

  • Horseradish Peroxidase as a catalyst for atom transfer radical polymerization
    Macromolecular Rapid Communications, 2011
    Co-Authors: Severin J Sigg, Farzad Seidi, Kasper Renggli, Tilana B Silva, Gergely Kali, Nico Bruns
    Abstract:

    The hemoprotein Horseradish Peroxidase (HRP) catalyzes the polymn. of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymn. (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indexes (PDIs) as low as 1.44 are obtained. The polymn. follows first order kinetics, but the evolution of mol. wt. and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, ?Mn and PDI depend on the pH and on the concn. of the reducing agent, sodium ascorbate. HRP is stable during the polymn. and does not unfold or form conjugates.

  • Horseradish Peroxidase as a catalyst for atom transfer radical polymerization
    Macromolecular Rapid Communications, 2011
    Co-Authors: Severin J Sigg, Farzad Seidi, Kasper Renggli, Tilana B Silva, Gergely Kali, Nico Bruns
    Abstract:

    The hemoprotein Horseradish Peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.44 are obtained. The polymerization follows first order kinetics, but the evolution of molecular weight and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, M(n) and PDI depend on the pH and on the concentration of the reducing agent, sodium ascorbate. HRP is stable during the polymerization and does not unfold or form conjugates.

William C De Groat - One of the best experts on this subject based on the ideXlab platform.

Severin J Sigg - One of the best experts on this subject based on the ideXlab platform.

  • Horseradish Peroxidase as a catalyst for atom transfer radical polymerization
    Macromolecular Rapid Communications, 2011
    Co-Authors: Severin J Sigg, Farzad Seidi, Kasper Renggli, Tilana B Silva, Gergely Kali, Nico Bruns
    Abstract:

    The hemoprotein Horseradish Peroxidase (HRP) catalyzes the polymn. of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymn. (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indexes (PDIs) as low as 1.44 are obtained. The polymn. follows first order kinetics, but the evolution of mol. wt. and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, ?Mn and PDI depend on the pH and on the concn. of the reducing agent, sodium ascorbate. HRP is stable during the polymn. and does not unfold or form conjugates.

  • Horseradish Peroxidase as a catalyst for atom transfer radical polymerization
    Macromolecular Rapid Communications, 2011
    Co-Authors: Severin J Sigg, Farzad Seidi, Kasper Renggli, Tilana B Silva, Gergely Kali, Nico Bruns
    Abstract:

    The hemoprotein Horseradish Peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.44 are obtained. The polymerization follows first order kinetics, but the evolution of molecular weight and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, M(n) and PDI depend on the pH and on the concentration of the reducing agent, sodium ascorbate. HRP is stable during the polymerization and does not unfold or form conjugates.

M.n. Kruse - One of the best experts on this subject based on the ideXlab platform.

Gergely Kali - One of the best experts on this subject based on the ideXlab platform.

  • Horseradish Peroxidase as a catalyst for atom transfer radical polymerization
    Macromolecular Rapid Communications, 2011
    Co-Authors: Severin J Sigg, Farzad Seidi, Kasper Renggli, Tilana B Silva, Gergely Kali, Nico Bruns
    Abstract:

    The hemoprotein Horseradish Peroxidase (HRP) catalyzes the polymn. of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymn. (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indexes (PDIs) as low as 1.44 are obtained. The polymn. follows first order kinetics, but the evolution of mol. wt. and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, ?Mn and PDI depend on the pH and on the concn. of the reducing agent, sodium ascorbate. HRP is stable during the polymn. and does not unfold or form conjugates.

  • Horseradish Peroxidase as a catalyst for atom transfer radical polymerization
    Macromolecular Rapid Communications, 2011
    Co-Authors: Severin J Sigg, Farzad Seidi, Kasper Renggli, Tilana B Silva, Gergely Kali, Nico Bruns
    Abstract:

    The hemoprotein Horseradish Peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.44 are obtained. The polymerization follows first order kinetics, but the evolution of molecular weight and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, M(n) and PDI depend on the pH and on the concentration of the reducing agent, sodium ascorbate. HRP is stable during the polymerization and does not unfold or form conjugates.